JP2003504046A - グルコアミラーゼ変異体 - Google Patents
グルコアミラーゼ変異体Info
- Publication number
- JP2003504046A JP2003504046A JP2001509477A JP2001509477A JP2003504046A JP 2003504046 A JP2003504046 A JP 2003504046A JP 2001509477 A JP2001509477 A JP 2001509477A JP 2001509477 A JP2001509477 A JP 2001509477A JP 2003504046 A JP2003504046 A JP 2003504046A
- Authority
- JP
- Japan
- Prior art keywords
- glucoamylase
- variant
- amino acid
- acid sequence
- parent
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 102100022624 Glucoamylase Human genes 0.000 title claims abstract description 157
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 title claims abstract description 155
- 230000000694 effects Effects 0.000 claims abstract description 48
- 230000001965 increasing effect Effects 0.000 claims abstract description 10
- 238000000034 method Methods 0.000 claims description 70
- 108020004414 DNA Proteins 0.000 claims description 30
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 29
- 102000004190 Enzymes Human genes 0.000 claims description 28
- 108090000790 Enzymes Proteins 0.000 claims description 28
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 28
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 24
- 229920002472 Starch Polymers 0.000 claims description 23
- 239000008107 starch Substances 0.000 claims description 23
- 235000019698 starch Nutrition 0.000 claims description 23
- 235000001014 amino acid Nutrition 0.000 claims description 21
- 239000013598 vector Substances 0.000 claims description 21
- 150000001413 amino acids Chemical class 0.000 claims description 18
- 238000006243 chemical reaction Methods 0.000 claims description 17
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims description 15
- 108090000637 alpha-Amylases Proteins 0.000 claims description 15
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 claims description 15
- 241000228212 Aspergillus Species 0.000 claims description 14
- 238000004519 manufacturing process Methods 0.000 claims description 14
- 150000007523 nucleic acids Chemical group 0.000 claims description 12
- 241000193830 Bacillus <bacterium> Species 0.000 claims description 11
- 238000012217 deletion Methods 0.000 claims description 11
- 230000037430 deletion Effects 0.000 claims description 11
- 239000013604 expression vector Substances 0.000 claims description 11
- 239000008103 glucose Substances 0.000 claims description 11
- 230000004048 modification Effects 0.000 claims description 11
- 238000012986 modification Methods 0.000 claims description 11
- 229910052799 carbon Inorganic materials 0.000 claims description 10
- 229910052757 nitrogen Inorganic materials 0.000 claims description 10
- 238000006467 substitution reaction Methods 0.000 claims description 10
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 9
- 238000000855 fermentation Methods 0.000 claims description 8
- 230000004151 fermentation Effects 0.000 claims description 8
- 229910052731 fluorine Inorganic materials 0.000 claims description 7
- 229910052698 phosphorus Inorganic materials 0.000 claims description 7
- 229910052717 sulfur Inorganic materials 0.000 claims description 7
- 241000894006 Bacteria Species 0.000 claims description 6
- 229920002774 Maltodextrin Polymers 0.000 claims description 6
- 238000003780 insertion Methods 0.000 claims description 6
- 230000037431 insertion Effects 0.000 claims description 6
- 239000007787 solid Substances 0.000 claims description 6
- 239000006188 syrup Substances 0.000 claims description 6
- 235000020357 syrup Nutrition 0.000 claims description 6
- 102220466851 HLA class II histocompatibility antigen, DR beta 4 chain_V59A_mutation Human genes 0.000 claims description 5
- 239000005913 Maltodextrin Substances 0.000 claims description 5
- 229940035034 maltodextrin Drugs 0.000 claims description 5
- 244000005700 microbiome Species 0.000 claims description 5
- 150000002482 oligosaccharides Chemical class 0.000 claims description 5
- 102220095362 rs876658893 Human genes 0.000 claims description 5
- 241000233866 Fungi Species 0.000 claims description 4
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims description 4
- 108010028688 Isoamylase Proteins 0.000 claims description 4
- 230000000295 complement effect Effects 0.000 claims description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 3
- 235000013922 glutamic acid Nutrition 0.000 claims description 3
- 239000004220 glutamic acid Substances 0.000 claims description 3
- 239000004472 Lysine Substances 0.000 claims description 2
- 230000035622 drinking Effects 0.000 claims description 2
- 239000000446 fuel Substances 0.000 claims description 2
- 229920001542 oligosaccharide Polymers 0.000 claims description 2
- 238000003259 recombinant expression Methods 0.000 claims description 2
- 241000228341 Talaromyces Species 0.000 claims 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 claims 3
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 claims 2
- 241001134780 Bacillus acidopullulyticus Species 0.000 claims 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims 1
- 241000589516 Pseudomonas Species 0.000 claims 1
- 241001453300 Pseudomonas amyloderamosa Species 0.000 claims 1
- 229960005070 ascorbic acid Drugs 0.000 claims 1
- 235000010323 ascorbic acid Nutrition 0.000 claims 1
- 239000011668 ascorbic acid Substances 0.000 claims 1
- 235000013361 beverage Nutrition 0.000 claims 1
- 239000003518 caustics Substances 0.000 claims 1
- 239000008121 dextrose Substances 0.000 claims 1
- 150000002894 organic compounds Chemical class 0.000 claims 1
- 102220092092 rs876657864 Human genes 0.000 claims 1
- 230000002538 fungal effect Effects 0.000 abstract description 8
- 108090000623 proteins and genes Proteins 0.000 description 31
- 210000004027 cell Anatomy 0.000 description 30
- 230000035772 mutation Effects 0.000 description 30
- 239000012634 fragment Substances 0.000 description 28
- 229940088598 enzyme Drugs 0.000 description 27
- 239000002773 nucleotide Substances 0.000 description 20
- 125000003729 nucleotide group Chemical group 0.000 description 20
- 241000223218 Fusarium Species 0.000 description 17
- 239000013612 plasmid Substances 0.000 description 16
- 229940024606 amino acid Drugs 0.000 description 15
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 14
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 14
- 108090000765 processed proteins & peptides Proteins 0.000 description 14
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 13
- 229920001184 polypeptide Polymers 0.000 description 13
- 102000004196 processed proteins & peptides Human genes 0.000 description 13
- 239000000523 sample Substances 0.000 description 13
- 239000001632 sodium acetate Substances 0.000 description 13
- 235000017281 sodium acetate Nutrition 0.000 description 13
- 239000000758 substrate Substances 0.000 description 13
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 description 12
- 239000000463 material Substances 0.000 description 12
- 125000000539 amino acid group Chemical group 0.000 description 11
- 235000018102 proteins Nutrition 0.000 description 11
- 102000004169 proteins and genes Human genes 0.000 description 11
- 239000000243 solution Substances 0.000 description 11
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 10
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 10
- 102000004139 alpha-Amylases Human genes 0.000 description 10
- 229940024171 alpha-amylase Drugs 0.000 description 10
- 238000003752 polymerase chain reaction Methods 0.000 description 10
- 210000001938 protoplast Anatomy 0.000 description 10
- 241000228245 Aspergillus niger Species 0.000 description 9
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 9
- 238000011282 treatment Methods 0.000 description 9
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 8
- 108091034117 Oligonucleotide Proteins 0.000 description 8
- 239000002299 complementary DNA Substances 0.000 description 8
- 238000010276 construction Methods 0.000 description 8
- 239000000203 mixture Substances 0.000 description 8
- 230000008569 process Effects 0.000 description 8
- 238000002708 random mutagenesis Methods 0.000 description 8
- 108050008938 Glucoamylases Proteins 0.000 description 7
- 101000757144 Aspergillus niger Glucoamylase Proteins 0.000 description 6
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 6
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 6
- 238000011534 incubation Methods 0.000 description 6
- 229940081969 saccharomyces cerevisiae Drugs 0.000 description 6
- 238000002741 site-directed mutagenesis Methods 0.000 description 6
- 229920002245 Dextrose equivalent Polymers 0.000 description 5
- 241000588724 Escherichia coli Species 0.000 description 5
- NPPQSCRMBWNHMW-UHFFFAOYSA-N Meprobamate Chemical compound NC(=O)OCC(C)(CCC)COC(N)=O NPPQSCRMBWNHMW-UHFFFAOYSA-N 0.000 description 5
- 239000002033 PVDF binder Substances 0.000 description 5
- 235000004279 alanine Nutrition 0.000 description 5
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 5
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 5
- 235000011130 ammonium sulphate Nutrition 0.000 description 5
- 239000000872 buffer Substances 0.000 description 5
- 238000005119 centrifugation Methods 0.000 description 5
- 230000008859 change Effects 0.000 description 5
- 230000007062 hydrolysis Effects 0.000 description 5
- 238000006460 hydrolysis reaction Methods 0.000 description 5
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 5
- 230000009466 transformation Effects 0.000 description 5
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 4
- 229920000936 Agarose Polymers 0.000 description 4
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 4
- 108020004705 Codon Proteins 0.000 description 4
- 241000282326 Felis catus Species 0.000 description 4
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 4
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 4
- 108091005804 Peptidases Proteins 0.000 description 4
- GLUUGHFHXGJENI-UHFFFAOYSA-N Piperazine Chemical compound C1CNCCN1 GLUUGHFHXGJENI-UHFFFAOYSA-N 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 102000005924 Triose-Phosphate Isomerase Human genes 0.000 description 4
- 108700015934 Triose-phosphate isomerases Proteins 0.000 description 4
- 239000001166 ammonium sulphate Substances 0.000 description 4
- 229960000723 ampicillin Drugs 0.000 description 4
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 4
- 102220421966 c.196C>G Human genes 0.000 description 4
- 239000012876 carrier material Substances 0.000 description 4
- 230000029087 digestion Effects 0.000 description 4
- 238000009826 distribution Methods 0.000 description 4
- 238000001914 filtration Methods 0.000 description 4
- 230000006870 function Effects 0.000 description 4
- 238000009396 hybridization Methods 0.000 description 4
- 238000005259 measurement Methods 0.000 description 4
- 231100000350 mutagenesis Toxicity 0.000 description 4
- 239000002853 nucleic acid probe Substances 0.000 description 4
- 238000012216 screening Methods 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 239000000725 suspension Substances 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 3
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 3
- 108010065511 Amylases Proteins 0.000 description 3
- 101000961203 Aspergillus awamori Glucoamylase Proteins 0.000 description 3
- 240000006439 Aspergillus oryzae Species 0.000 description 3
- 235000002247 Aspergillus oryzae Nutrition 0.000 description 3
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 3
- 241000194108 Bacillus licheniformis Species 0.000 description 3
- 235000014469 Bacillus subtilis Nutrition 0.000 description 3
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 3
- 102000004594 DNA Polymerase I Human genes 0.000 description 3
- 108010017826 DNA Polymerase I Proteins 0.000 description 3
- 229930091371 Fructose Natural products 0.000 description 3
- 239000005715 Fructose Substances 0.000 description 3
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 description 3
- 241000221779 Fusarium sambucinum Species 0.000 description 3
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 3
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 239000012901 Milli-Q water Substances 0.000 description 3
- 239000000020 Nitrocellulose Substances 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 3
- 241000235403 Rhizomucor miehei Species 0.000 description 3
- 108700040099 Xylose isomerases Proteins 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 125000003295 alanine group Chemical class N[C@@H](C)C(=O)* 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 210000000349 chromosome Anatomy 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 238000012258 culturing Methods 0.000 description 3
- 239000013613 expression plasmid Substances 0.000 description 3
- 238000003348 filter assay Methods 0.000 description 3
- 150000004676 glycans Chemical class 0.000 description 3
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 3
- 235000019341 magnesium sulphate Nutrition 0.000 description 3
- 239000003550 marker Substances 0.000 description 3
- 238000002703 mutagenesis Methods 0.000 description 3
- 229920001220 nitrocellulos Polymers 0.000 description 3
- 229920001282 polysaccharide Polymers 0.000 description 3
- 239000005017 polysaccharide Substances 0.000 description 3
- 235000019419 proteases Nutrition 0.000 description 3
- 239000000600 sorbitol Substances 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- SNBCLPGEMZEWLU-QXFUBDJGSA-N 2-chloro-n-[[(2r,3s,5r)-3-hydroxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methyl]acetamide Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CNC(=O)CCl)[C@@H](O)C1 SNBCLPGEMZEWLU-QXFUBDJGSA-N 0.000 description 2
- DLFVBJFMPXGRIB-UHFFFAOYSA-N Acetamide Chemical compound CC(N)=O DLFVBJFMPXGRIB-UHFFFAOYSA-N 0.000 description 2
- 108091093088 Amplicon Proteins 0.000 description 2
- 239000004382 Amylase Substances 0.000 description 2
- 102000013142 Amylases Human genes 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- 241000351920 Aspergillus nidulans Species 0.000 description 2
- 241000193749 Bacillus coagulans Species 0.000 description 2
- 241000194107 Bacillus megaterium Species 0.000 description 2
- 244000063299 Bacillus subtilis Species 0.000 description 2
- 108091005658 Basic proteases Proteins 0.000 description 2
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 2
- 241000193764 Brevibacillus brevis Species 0.000 description 2
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 2
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
- 101100364969 Dictyostelium discoideum scai gene Proteins 0.000 description 2
- -1 E Inorganic materials 0.000 description 2
- 241000223195 Fusarium graminearum Species 0.000 description 2
- 241000567178 Fusarium venenatum Species 0.000 description 2
- 108090001060 Lipase Proteins 0.000 description 2
- PKVZBNCYEICAQP-UHFFFAOYSA-N Mecamylamine hydrochloride Chemical compound Cl.C1CC2C(C)(C)C(NC)(C)C1C2 PKVZBNCYEICAQP-UHFFFAOYSA-N 0.000 description 2
- 101100364971 Mus musculus Scai gene Proteins 0.000 description 2
- 102220519841 Putative neutrophil cytosol factor 1B_S30P_mutation Human genes 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 241000235070 Saccharomyces Species 0.000 description 2
- 241000235346 Schizosaccharomyces Species 0.000 description 2
- 108091081021 Sense strand Proteins 0.000 description 2
- 238000002105 Southern blotting Methods 0.000 description 2
- 241000187747 Streptomyces Species 0.000 description 2
- 241000187432 Streptomyces coelicolor Species 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 101150069003 amdS gene Proteins 0.000 description 2
- 235000019418 amylase Nutrition 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 229960001230 asparagine Drugs 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N aspartic acid group Chemical group N[C@@H](CC(=O)O)C(=O)O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- 229940054340 bacillus coagulans Drugs 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 239000001110 calcium chloride Substances 0.000 description 2
- 229910001628 calcium chloride Inorganic materials 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
- 238000006555 catalytic reaction Methods 0.000 description 2
- 229920002301 cellulose acetate Polymers 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- LXBIFEVIBLOUGU-JGWLITMVSA-N duvoglustat Chemical compound OC[C@H]1NC[C@H](O)[C@@H](O)[C@@H]1O LXBIFEVIBLOUGU-JGWLITMVSA-N 0.000 description 2
- 108010030074 endodeoxyribonuclease MluI Proteins 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 239000006167 equilibration buffer Substances 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 235000019534 high fructose corn syrup Nutrition 0.000 description 2
- 230000010354 integration Effects 0.000 description 2
- 230000035800 maturation Effects 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- 229910000403 monosodium phosphate Inorganic materials 0.000 description 2
- 235000019799 monosodium phosphate Nutrition 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 150000008300 phosphoramidites Chemical class 0.000 description 2
- 230000008488 polyadenylation Effects 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 102200115808 rs10127939 Human genes 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- AJPJDKMHJJGVTQ-UHFFFAOYSA-M sodium dihydrogen phosphate Chemical compound [Na+].OP(O)([O-])=O AJPJDKMHJJGVTQ-UHFFFAOYSA-M 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- XUFXOAAUWZOOIT-SXARVLRPSA-N (2R,3R,4R,5S,6R)-5-[[(2R,3R,4R,5S,6R)-5-[[(2R,3R,4S,5S,6R)-3,4-dihydroxy-6-methyl-5-[[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)-1-cyclohex-2-enyl]amino]-2-oxanyl]oxy]-3,4-dihydroxy-6-(hydroxymethyl)-2-oxanyl]oxy]-6-(hydroxymethyl)oxane-2,3,4-triol Chemical compound O([C@H]1O[C@H](CO)[C@H]([C@@H]([C@H]1O)O)O[C@H]1O[C@@H]([C@H]([C@H](O)[C@H]1O)N[C@@H]1[C@@H]([C@@H](O)[C@H](O)C(CO)=C1)O)C)[C@@H]1[C@@H](CO)O[C@@H](O)[C@H](O)[C@H]1O XUFXOAAUWZOOIT-SXARVLRPSA-N 0.000 description 1
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- IFBHRQDFSNCLOZ-RMPHRYRLSA-N 4-nitrophenyl beta-D-glucoside Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=CC=C([N+]([O-])=O)C=C1 IFBHRQDFSNCLOZ-RMPHRYRLSA-N 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 102100039109 Amelogenin, Y isoform Human genes 0.000 description 1
- 241000636501 Asparagus aspergillus Species 0.000 description 1
- 241001513093 Aspergillus awamori Species 0.000 description 1
- 101100316860 Autographa californica nuclear polyhedrosis virus DA18 gene Proteins 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 241000193752 Bacillus circulans Species 0.000 description 1
- 241000193422 Bacillus lentus Species 0.000 description 1
- 241000193388 Bacillus thuringiensis Species 0.000 description 1
- 241000510930 Brachyspira pilosicoli Species 0.000 description 1
- 241000122205 Chamaeleonidae Species 0.000 description 1
- 229920002261 Corn starch Polymers 0.000 description 1
- LXJXRIRHZLFYRP-VKHMYHEASA-N D-glyceraldehyde 3-phosphate Chemical compound O=C[C@H](O)COP(O)(O)=O LXJXRIRHZLFYRP-VKHMYHEASA-N 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 239000003298 DNA probe Substances 0.000 description 1
- LXBIFEVIBLOUGU-UHFFFAOYSA-N Deoxymannojirimycin Natural products OCC1NCC(O)C(O)C1O LXBIFEVIBLOUGU-UHFFFAOYSA-N 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 241000192125 Firmicutes Species 0.000 description 1
- 241000145614 Fusarium bactridioides Species 0.000 description 1
- 241000567163 Fusarium cerealis Species 0.000 description 1
- 101150094690 GAL1 gene Proteins 0.000 description 1
- 102100028501 Galanin peptides Human genes 0.000 description 1
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 1
- 206010071602 Genetic polymorphism Diseases 0.000 description 1
- 101100001650 Geobacillus stearothermophilus amyM gene Proteins 0.000 description 1
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Natural products NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 102100036738 Guanine nucleotide-binding protein subunit alpha-11 Human genes 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101100378966 Homo sapiens AMELY gene Proteins 0.000 description 1
- 101100121078 Homo sapiens GAL gene Proteins 0.000 description 1
- 101100283445 Homo sapiens GNA11 gene Proteins 0.000 description 1
- 102000004195 Isomerases Human genes 0.000 description 1
- 108090000769 Isomerases Proteins 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241000194109 Paenibacillus lautus Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 101100219325 Phaseolus vulgaris BA13 gene Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 229920001030 Polyethylene Glycol 4000 Polymers 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- 108020004518 RNA Probes Proteins 0.000 description 1
- 239000003391 RNA probe Substances 0.000 description 1
- 101001062854 Rattus norvegicus Fatty acid-binding protein 5 Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 241000554265 Sphaerias Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 241000187398 Streptomyces lividans Species 0.000 description 1
- 241001468239 Streptomyces murinus Species 0.000 description 1
- 241000187180 Streptomyces sp. Species 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 101100157012 Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485) xynB gene Proteins 0.000 description 1
- 102220544598 Tyrosinase_S44G_mutation Human genes 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- 229960002632 acarbose Drugs 0.000 description 1
- XUFXOAAUWZOOIT-UHFFFAOYSA-N acarviostatin I01 Natural products OC1C(O)C(NC2C(C(O)C(O)C(CO)=C2)O)C(C)OC1OC(C(C1O)O)C(CO)OC1OC1C(CO)OC(O)C(O)C1O XUFXOAAUWZOOIT-UHFFFAOYSA-N 0.000 description 1
- 108010048241 acetamidase Proteins 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 108010045649 agarase Proteins 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- BNABBHGYYMZMOA-AHIHXIOASA-N alpha-maltoheptaose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)O[C@H](O[C@@H]2[C@H](O[C@H](O[C@@H]3[C@H](O[C@H](O[C@@H]4[C@H](O[C@H](O[C@@H]5[C@H](O[C@H](O[C@@H]6[C@H](O[C@H](O)[C@H](O)[C@H]6O)CO)[C@H](O)[C@H]5O)CO)[C@H](O)[C@H]4O)CO)[C@H](O)[C@H]3O)CO)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O BNABBHGYYMZMOA-AHIHXIOASA-N 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000008122 artificial sweetener Substances 0.000 description 1
- 235000021311 artificial sweeteners Nutrition 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 235000020054 awamori Nutrition 0.000 description 1
- 229940097012 bacillus thuringiensis Drugs 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 229910021538 borax Inorganic materials 0.000 description 1
- 125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 239000008120 corn starch Substances 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000006240 deamidation Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 235000021433 fructose syrup Nutrition 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 125000003147 glycosyl group Chemical group 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000003262 industrial enzyme Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 238000009434 installation Methods 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 238000012933 kinetic analysis Methods 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 101150095344 niaD gene Proteins 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 239000002751 oligonucleotide probe Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 235000004252 protein component Nutrition 0.000 description 1
- 101150054232 pyrG gene Proteins 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 102220219006 rs1060501597 Human genes 0.000 description 1
- 102220217183 rs1060504842 Human genes 0.000 description 1
- 102200148528 rs587776998 Human genes 0.000 description 1
- 102220219774 rs764111950 Human genes 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 238000012807 shake-flask culturing Methods 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- FQENQNTWSFEDLI-UHFFFAOYSA-J sodium diphosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])([O-])=O FQENQNTWSFEDLI-UHFFFAOYSA-J 0.000 description 1
- 229940048086 sodium pyrophosphate Drugs 0.000 description 1
- 235000010339 sodium tetraborate Nutrition 0.000 description 1
- 238000011146 sterile filtration Methods 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 239000012089 stop solution Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 239000008399 tap water Substances 0.000 description 1
- 235000020679 tap water Nutrition 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 235000019818 tetrasodium diphosphate Nutrition 0.000 description 1
- 239000001577 tetrasodium phosphonato phosphate Substances 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- BSVBQGMMJUBVOD-UHFFFAOYSA-N trisodium borate Chemical compound [Na+].[Na+].[Na+].[O-]B([O-])[O-] BSVBQGMMJUBVOD-UHFFFAOYSA-N 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 101150110790 xylB gene Proteins 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2428—Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/20—Preparation of compounds containing saccharide radicals produced by the action of an exo-1,4 alpha-glucosidase, e.g. dextrose
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02E—REDUCTION OF GREENHOUSE GAS [GHG] EMISSIONS, RELATED TO ENERGY GENERATION, TRANSMISSION OR DISTRIBUTION
- Y02E50/00—Technologies for the production of fuel of non-fossil origin
- Y02E50/10—Biofuels, e.g. bio-diesel
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Health & Medical Sciences (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DKPA199900999 | 1999-07-09 | ||
| DK199900999 | 1999-07-09 | ||
| PCT/DK2000/000373 WO2001004273A2 (en) | 1999-07-09 | 2000-07-07 | Glucoamylase variant |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2003504046A true JP2003504046A (ja) | 2003-02-04 |
| JP2003504046A5 JP2003504046A5 (https=) | 2007-08-02 |
Family
ID=8099879
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2001509477A Pending JP2003504046A (ja) | 1999-07-09 | 2000-07-07 | グルコアミラーゼ変異体 |
Country Status (8)
| Country | Link |
|---|---|
| US (3) | US7354753B2 (https=) |
| EP (2) | EP1200566A2 (https=) |
| JP (1) | JP2003504046A (https=) |
| CN (2) | CN100510067C (https=) |
| AR (2) | AR029759A1 (https=) |
| AU (1) | AU5805700A (https=) |
| CA (1) | CA2374009A1 (https=) |
| WO (1) | WO2001004273A2 (https=) |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007509630A (ja) * | 2003-10-28 | 2007-04-19 | ノボザイムス ノース アメリカ,インコーポレイティド | ハイブリッド酵素 |
| JP2008505632A (ja) * | 2004-07-07 | 2008-02-28 | ダニスコ エイ/エス | 非マルトース生成エキソアミラーゼ改変体 |
| CN100443589C (zh) * | 2005-12-30 | 2008-12-17 | 湖南鸿鹰祥生物工程股份有限公司 | 高转化率高纯度糖化酶浓缩液的生产方法 |
| JP2011500020A (ja) * | 2007-10-09 | 2011-01-06 | ダニスコ・ユーエス・インク | 性質が変えられたグルコアミラーゼ変異種 |
| JP2011502543A (ja) * | 2007-11-20 | 2011-01-27 | ダニスコ・ユーエス・インク | 変更された性質を有するグルコアミラーゼ変異体 |
Families Citing this family (111)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6352851B1 (en) * | 1998-07-15 | 2002-03-05 | Novozymes A/S | Glucoamylase variants |
| CN100510067C (zh) * | 1999-07-09 | 2009-07-08 | 诺维信公司 | 葡糖淀粉酶变体 |
| EP1370648A2 (en) | 2000-08-01 | 2003-12-17 | Novozymes A/S | Alpha-amylase mutants with altered properties |
| EP2159279A3 (en) | 2001-05-15 | 2010-05-12 | Novozymes A/S | Alpha-amylase variant with altered properties |
| AU2002333212A1 (en) * | 2001-10-01 | 2003-04-14 | Novozymes A/S | Glucoamylase variants |
| JP4897186B2 (ja) * | 2002-03-27 | 2012-03-14 | 花王株式会社 | 変異アルカリセルラーゼ |
| JP4550587B2 (ja) | 2002-12-17 | 2010-09-22 | ノボザイムス アクティーゼルスカブ | 熱安定性α−アミラーゼ |
| US7579177B2 (en) | 2003-05-30 | 2009-08-25 | Novozymes A/S | Alcohol product processes |
| US8143048B2 (en) | 2003-07-07 | 2012-03-27 | Danisco A/S | Exo-specific amylase polypeptides, nucleic acids encoding those polypeptides and uses thereof |
| KR101286991B1 (ko) | 2003-07-07 | 2013-07-23 | 듀폰 뉴트리션 바이오사이언시즈 에이피에스 | 엑소-특이성 아밀라아제 폴리펩티드, 그 폴리펩티드를코딩하는 핵산 및 그의 용도 |
| DE102004026152A1 (de) * | 2004-05-28 | 2005-12-15 | Basf Ag | Fermentative Herstellung von Feinchemikalien |
| EP2365068B1 (en) | 2004-12-22 | 2017-03-01 | Novozymes A/S | Enzymes for starch processing |
| US8030050B2 (en) | 2005-07-07 | 2011-10-04 | Danisco A/S | Modified amylases from Pseudomonas species |
| CN101268195A (zh) | 2005-09-20 | 2008-09-17 | 诺维信北美公司 | 产生发酵产物的方法 |
| WO2007076388A2 (en) | 2005-12-22 | 2007-07-05 | Novozymes North America, Inc. | Processes for producing a fermentation product |
| CN101405397A (zh) | 2006-03-22 | 2009-04-08 | 诺维信北美公司 | 发酵方法 |
| ES2644745T3 (es) | 2006-06-19 | 2017-11-30 | Dupont Nutrition Biosciences Aps | Polipéptido |
| CN101522893B (zh) | 2006-10-10 | 2014-07-09 | 丹尼斯科美国公司 | 具有改变性质的葡糖淀粉酶变体 |
| ES2748245T3 (es) | 2007-04-24 | 2020-03-16 | Novozymes North America Inc | Detoxificación de materiales que contienen lignocelulosa pretratados |
| WO2009030713A1 (en) | 2007-09-03 | 2009-03-12 | Novozymes A/S | Detoxifying and recycling of washing solution used in pretreatment of lignocellulose-containing materials |
| US8592194B2 (en) | 2007-10-09 | 2013-11-26 | Danisco Us Inc. | Glucoamylase variants with altered properties |
| EP2281036B1 (en) * | 2008-04-18 | 2013-02-27 | New England Biolabs, Inc. | Endoglyosidases that cleave o-linked glycans |
| CN102057040A (zh) | 2008-06-06 | 2011-05-11 | 丹尼斯科美国公司 | 具有改良特性的嗜热脂肪土芽孢杆菌α-淀粉酶(AMYS)变体 |
| US20110097779A1 (en) | 2008-06-23 | 2011-04-28 | Chee-Leong Soong | Processes for Producing Fermentation Products |
| BRPI0919525A2 (pt) | 2008-09-30 | 2015-08-18 | Novozymes North America Inc | Métodos para produzir um produto de fermentação a partir de um material contendo lignocelulose, para intensificar hidrólise enzimática e para reduzir o efeito prejudicial de lignina na hidrólise de um material contendo lignocelulose, e, produto de fermentação |
| CN102292444A (zh) | 2008-11-20 | 2011-12-21 | 诺维信股份有限公司 | 具有淀粉分解增强活性的多肽和编码该多肽的多核苷酸 |
| US20120028299A1 (en) | 2008-12-30 | 2012-02-02 | Novozymes North America, Inc. | Enzymatic Hydrolysis Of Pretreated Lignocellulose-Containing Material With Dissolved Air Flotation Sludge |
| WO2010078392A2 (en) | 2008-12-31 | 2010-07-08 | Novozymes North America, Inc. | Processes of producing fermentation products |
| BRPI1014799A2 (pt) | 2009-07-07 | 2015-08-25 | Novozymes As | Processo para hidrolisar material de planta, e, recipiente |
| CN102498401B (zh) | 2009-07-17 | 2015-12-02 | 诺维信公司 | 在纤维素材料水解中分析纤维素衰变的方法 |
| AR077942A1 (es) * | 2009-08-19 | 2011-10-05 | Danisco | Variantes de glucoamilasa |
| CN102665425A (zh) | 2009-09-30 | 2012-09-12 | 诺维信公司 | 馒头制备方法和馒头改进组合物 |
| CN102933227A (zh) | 2009-12-22 | 2013-02-13 | 诺维信公司 | 包含增强性多肽和淀粉降解酶的组合物及其用途 |
| US20130040354A1 (en) | 2010-01-29 | 2013-02-14 | Novozymes A/S | Biogas Production Process With Enzymatic Pre-Treatment |
| WO2011100161A1 (en) | 2010-02-09 | 2011-08-18 | Novozymes North America, Inc. | Addition of alpha - glucosidase and cobalt for producing fermentation products from starch |
| EP2553111B1 (en) | 2010-03-30 | 2016-05-11 | Novozymes A/S | Methods for enhancing by-products from fermentation processes |
| MX338068B (es) | 2010-04-14 | 2016-04-01 | Novozymes As | Polipeptidos que tienen actividad de glucoamilasa y polinucleotidos que codifican los mismos. |
| CA2802083C (en) | 2010-06-11 | 2018-10-09 | Novozymes A/S | Enzymatic flour correction |
| US9308064B2 (en) | 2010-07-26 | 2016-04-12 | Johnson & Johnson Consumer Inc. | Devices and methods for collecting and analyzing fluid samples from the oral cavity |
| US20130157307A1 (en) | 2010-08-02 | 2013-06-20 | Novozymes North America, Inc. | Process of Producing A Fermentation Product |
| US9057087B2 (en) | 2010-11-19 | 2015-06-16 | Novozymes North America, Inc. | Processes of producing a fermentation product |
| EP2654567B1 (en) | 2010-12-22 | 2018-04-04 | Novozymes North America, Inc. | Process for producing fermentation products from starch containing materials |
| EP2661499A1 (en) | 2011-01-04 | 2013-11-13 | Novozymes A/S | Process for producing biogas from pectin and lignocellulose containing material |
| US9677094B2 (en) | 2011-02-07 | 2017-06-13 | Novozymes A/S | Process of producing a fermentation product |
| MX2013014236A (es) | 2011-06-28 | 2014-01-23 | Novozymes As | Biogas a partir de bagazo tratado con enzimas. |
| ES2834102T3 (es) | 2011-06-30 | 2021-06-16 | Novozymes As | Variantes de alfa-amilasa |
| BR112014000143B1 (pt) | 2011-07-06 | 2021-04-06 | Novozymes A/S | Variante de alfa-amilase, polinucleotídeo isolado, vetor de expressão, célula hospedeira, métodos de produzir uma variante de alfa-amilase, para produzir um produto de fermentação a partir de um material contendo amido, e, para a produção um derivado de amido enzimaticamente modificado |
| EP2734633B1 (en) | 2011-07-22 | 2019-05-01 | Novozymes North America, Inc. | Processes for pretreating cellulosic material and improving hydrolysis thereof |
| EP2742350B1 (en) | 2011-08-08 | 2019-10-30 | The Coca-Cola Company | Cell lines comprising endogenous taste receptors and their uses |
| MX353581B (es) | 2011-10-11 | 2018-01-19 | Novozymes North America Inc | Procesos para producir productos de fermentacion. |
| IN2014CN04905A (https=) | 2011-12-02 | 2015-09-18 | Novozymes As | |
| WO2013083801A2 (en) | 2011-12-09 | 2013-06-13 | Novozymes A/S | Biogas from substrates comprising animal manure and enzymes |
| EP2794899A1 (en) | 2011-12-21 | 2014-10-29 | Novozymes, Inc. | Methods for determining the degradation of a biomass material |
| ES2935920T3 (es) | 2012-03-30 | 2023-03-13 | Novozymes North America Inc | Procesos de elaboración de productos de fermentación |
| CN104334738B (zh) | 2012-03-30 | 2019-01-29 | 诺维信北美公司 | 生产发酵产物的方法 |
| US9828595B2 (en) | 2012-08-17 | 2017-11-28 | Novozymes A/S | Thermostable asparaginase variants and polynucleotides encoding same |
| WO2014039773A1 (en) * | 2012-09-07 | 2014-03-13 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same and uses thereof |
| CN104870631B (zh) * | 2012-12-11 | 2025-03-25 | 丹尼斯科美国公司 | 表达来自烟曲霉的葡糖淀粉酶的里氏木霉宿主细胞和其使用方法 |
| HUE040545T2 (hu) | 2013-07-17 | 2019-03-28 | Novozymes As | Pullulanáz kimérák és az azokat kódoló polinukleotidok |
| US9951364B2 (en) | 2013-09-11 | 2018-04-24 | Novozymes A/S | Processes for producing fermentation products |
| EP3415624B1 (en) | 2014-01-22 | 2021-08-04 | Novozymes A/S | Pullulanase variants and polynucleotides encoding same |
| EP3712240B1 (en) | 2014-02-07 | 2023-09-27 | Novozymes A/S | Compositions for producing glucose syrups |
| WO2015143144A1 (en) | 2014-03-19 | 2015-09-24 | Novozymes A/S | Method for enhancing activity of an x143 polypeptide |
| EP3129478B1 (en) | 2014-04-10 | 2019-03-27 | Novozymes A/S | Alpha-amylase variants and polynucleotides encoding same |
| BR112017000004B1 (pt) | 2014-07-08 | 2022-01-18 | Caravan Ingredients Inc | Produção de açúcar e métodos de confeitaria de melhoramento de textura e produtos formados a partir deles |
| WO2016062875A2 (en) | 2014-10-23 | 2016-04-28 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same |
| CA2967710A1 (en) | 2014-12-01 | 2016-06-09 | Novozymes A/S | Improved production of glucose syrups |
| US10676727B2 (en) | 2015-06-18 | 2020-06-09 | Novozymes A/S | Polypeptides having trehalase activity and the use thereof in process of producing fermentation products |
| CN108699570A (zh) | 2015-12-22 | 2018-10-23 | 诺维信公司 | 从酒糟水提取油的工艺 |
| US10067091B2 (en) | 2016-07-29 | 2018-09-04 | Saudi Arabian Oil Company | Integrated sediment and water analysis device and method |
| US11015212B2 (en) | 2016-10-17 | 2021-05-25 | Novozymes A/S | Methods of reducing foam during ethanol fermentation |
| US10889836B2 (en) | 2016-11-23 | 2021-01-12 | Novozymes A/S | Yeast for ethanol production |
| CN110651048A (zh) * | 2017-04-11 | 2020-01-03 | 诺维信公司 | 葡糖淀粉酶变体和编码它们的多核苷酸 |
| WO2018202880A1 (en) * | 2017-05-05 | 2018-11-08 | C-Lecta Gmbh | Glucose isomerase |
| WO2018222990A1 (en) | 2017-06-02 | 2018-12-06 | Novozymes A/S | Improved yeast for ethanol production |
| ES2908190T3 (es) | 2017-06-28 | 2022-04-28 | Novozymes As | Polipéptidos con actividad de trehalasa y polinucleótidos que los codifican |
| CA3070281A1 (en) | 2017-08-08 | 2019-02-14 | Novozymes A/S | Polypeptides having trehalase activity and the use thereof in process of producing fermentation products |
| US12227784B2 (en) | 2017-09-15 | 2025-02-18 | Novozymes A/S | Enzyme blends and processes for improving the nutritional quality of animal feed |
| BR112020007814A2 (pt) | 2017-10-23 | 2020-10-20 | Novozymes A/S | processos para reduzir e/ou prevenir um aumento nos níveis de ácido lático em um sistema de fermentação de biocombustível e para produção de um produto de fermentação a partir de um material contendo amido, e, uso de um polipeptídeo, ou uma composição enzimática |
| CA3089135A1 (en) | 2018-01-29 | 2019-08-01 | Novozymes A/S | Microorganisms with improved nitrogen utilization for ethanol production |
| US11473109B2 (en) | 2018-02-15 | 2022-10-18 | Novozymes A/S | Yeast for ethanol production |
| CA3098718A1 (en) | 2018-05-31 | 2019-12-05 | Novozymes A/S | Processes for enhancing yeast growth and productivity |
| WO2020014407A1 (en) | 2018-07-11 | 2020-01-16 | Novozymes A/S | Processes for producing fermentation products |
| BR112021001282A2 (pt) | 2018-07-25 | 2021-04-27 | Novozymes A/S | levedura expressando enzimas para produção de etanol |
| CA3114783A1 (en) | 2018-10-08 | 2020-04-16 | Novozymes A/S | Enzyme-expressing yeast for ethanol production |
| US11622751B2 (en) | 2018-12-19 | 2023-04-11 | Johnson & Johnson Consumer Inc. | Devices and methods for collecting saliva samples from the oral cavity |
| WO2020160126A1 (en) | 2019-01-31 | 2020-08-06 | Novozymes A/S | Polypeptides having xylanase activity and use thereof for improving the nutritional quality of animal feed |
| WO2020206058A1 (en) | 2019-04-02 | 2020-10-08 | Novozymes A/S | Process for producing a fermentation product |
| WO2021007379A1 (en) | 2019-07-09 | 2021-01-14 | Dupont Nutrition Biosciences Aps | Fat coated particulate enzyme compositions |
| EP4004029A1 (en) | 2019-07-26 | 2022-06-01 | Novozymes A/S | Microorganisms with improved nitrogen transport for ethanol production |
| BR112022002203A2 (pt) | 2019-08-05 | 2022-09-06 | Novozymes As | Misturas de enzimas e processos para produção de um ingrediente alimentar com alto teor de proteína a partir de um subproduto de vinhaça completa |
| MX2021015818A (es) | 2019-08-06 | 2022-02-03 | Novozymes As | Proteinas de fusion para mejorar la expresion de enzimas. |
| WO2021046073A1 (en) | 2019-09-05 | 2021-03-11 | Dupont Nutrition Biosciences Aps | Feed composition |
| CA3152952A1 (en) | 2019-09-16 | 2021-03-25 | Novozymes A/S | Polypeptides having beta-glucanase activity and polynucleotides encoding same |
| AU2020402990A1 (en) | 2019-12-10 | 2022-06-09 | Novozymes A/S | Microorganism for improved pentose fermentation |
| MX2022006438A (es) | 2019-12-16 | 2022-06-22 | Novozymes As | Procesos para obtener productos de fermentacion. |
| US20240228996A1 (en) | 2020-02-10 | 2024-07-11 | Novozymes A/S | Polypeptides having alpha-amylase activity and polynucleotides encoding same |
| WO2022090564A1 (en) | 2020-11-02 | 2022-05-05 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same |
| BR112023025624A2 (pt) | 2021-06-07 | 2024-02-27 | Novozymes As | Célula de levedura recombinante, célula hospedeira recombinante, composição, cocultura, métodos de produção de um derivado de uma célula hospedeira recombinante e de produção de um produto de fermentação, e, uso de uma célula hospedeira recombinante |
| CA3232987A1 (en) | 2021-09-27 | 2023-03-30 | Marion BERNARDEAU | Feed additive compositions and methods for using the same |
| CN119487187A (zh) * | 2021-10-15 | 2025-02-18 | 丹尼斯科美国公司 | 葡糖淀粉酶变体及其使用方法 |
| WO2023225510A1 (en) | 2022-05-17 | 2023-11-23 | Dupont Nutrition Biosciences Aps | Feed additive comprising enzyme combinations |
| EP4638725A1 (en) | 2022-12-19 | 2025-10-29 | Novozymes A/S | Carbohydrate esterase family 3 (ce3) polypeptides having acetyl xylan esterase activity and polynucleotides encoding same |
| WO2024137252A1 (en) | 2022-12-19 | 2024-06-27 | Novozymes A/S | Process for reducing syrup viscosity in the backend of a process for producing a fermentation product |
| CN120693401A (zh) | 2022-12-19 | 2025-09-23 | 诺维信公司 | 包含阿拉伯呋喃糖苷酶和木聚糖酶的组合物及其用于增加半纤维素纤维溶解的用途 |
| CN120380140A (zh) | 2022-12-19 | 2025-07-25 | 诺维信公司 | 具有阿魏酸酯酶和/或乙酰木聚糖酯酶活性的碳水化合物酯酶家族1(ce1)多肽和编码其的多核苷酸 |
| EP4638768A2 (en) | 2022-12-19 | 2025-10-29 | Novozymes A/S | Processes for producing fermentation products using fiber-degrading enzymes with engineered yeast |
| EP4701430A1 (en) | 2023-04-28 | 2026-03-04 | International N&H Denmark ApS | Ruminant feed additive compositions |
| AU2024303961A1 (en) | 2023-06-13 | 2025-12-11 | Novozymes A/S | Processes for producing fermentation products using engineered yeast expressing a beta-xylosidase |
| WO2025128568A1 (en) | 2023-12-11 | 2025-06-19 | Novozymes A/S | Composition and use thereof for increasing hemicellulosic fiber solubilization |
| WO2026008449A2 (en) | 2024-07-04 | 2026-01-08 | Novozymes A/S | A process for producing a fermentation product and a concentrated protein co-product |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH05507852A (ja) * | 1990-06-29 | 1993-11-11 | ノボザイムス アクティーゼルスカブ | 遺伝子工学処理をした酵素による澱粉のグルコースへの加水分解 |
| JP2002531121A (ja) * | 1998-12-07 | 2002-09-24 | ノボザイムス アクティーゼルスカブ | N末端伸長を有するグルコアミラーゼ |
| JP2007520047A (ja) * | 2004-01-28 | 2007-07-19 | 東京エレクトロン株式会社 | 大規模誘導結合プラズマ源用の小型な分布型誘導素子 |
Family Cites Families (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4272326A (en) | 1980-01-24 | 1981-06-09 | Allied Chemical Corporation | Enhanced distillation of cyclohexanol from phenol with additional cyclohexanone feed |
| US4760025A (en) | 1984-05-29 | 1988-07-26 | Genencor, Inc. | Modified enzymes and methods for making same |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| DK122686D0 (da) | 1986-03-17 | 1986-03-17 | Novo Industri As | Fremstilling af proteiner |
| JPS62272987A (ja) | 1986-05-22 | 1987-11-27 | Hitachi Plant Eng & Constr Co Ltd | ブドウ糖の製造方法 |
| DK463887D0 (da) | 1987-09-07 | 1987-09-07 | Novo Industri As | Gaerleader |
| JPH01191693A (ja) | 1988-01-25 | 1989-08-01 | Tdk Corp | デンプンの連続的糖化方法 |
| CA1333777C (en) | 1988-07-01 | 1995-01-03 | Randy M. Berka | Aspartic proteinase deficient filamentous fungi |
| JP2733330B2 (ja) | 1989-08-31 | 1998-03-30 | 日本食品化工株式会社 | 高純度澱粉糖の製造方法 |
| CA2038485A1 (en) | 1990-03-23 | 1991-09-24 | Donald K. Hadden | Nanofiltration process for making dextrose |
| CA2082279C (en) | 1990-05-09 | 2007-09-04 | Grethe Rasmussen | Cellulase preparation comprising an endoglucanase enzyme |
| US5231017A (en) | 1991-05-17 | 1993-07-27 | Solvay Enzymes, Inc. | Process for producing ethanol |
| US5665585A (en) * | 1992-09-03 | 1997-09-09 | Alko-Yhiot Oy | Recombinant production of glucoamylase P in trichoderma |
| US5605793A (en) | 1994-02-17 | 1997-02-25 | Affymax Technologies N.V. | Methods for in vitro recombination |
| DE4422198C2 (de) | 1994-06-24 | 1997-08-28 | Audi Ag | Verfahren zum Steuern der elektrischen Beheizung eines Katalysators |
| DK0894126T3 (da) | 1996-03-27 | 2006-06-12 | Novozymes As | Alkalisk phosphatase-deficient trådformet svamp |
| AU3892397A (en) * | 1996-07-24 | 1998-02-10 | Iowa State University Research Foundation Inc. | Protein engineering of glucoamylase to increase ph optimum, substrate specificity and thermostability |
| WO1999028448A1 (en) | 1997-11-26 | 1999-06-10 | Novo Nordisk A/S | Thermostable glucoamylase |
| US6255084B1 (en) * | 1997-11-26 | 2001-07-03 | Novozymes A/S | Thermostable glucoamylase |
| US6352851B1 (en) | 1998-07-15 | 2002-03-05 | Novozymes A/S | Glucoamylase variants |
| US6329186B1 (en) | 1998-12-07 | 2001-12-11 | Novozymes A/S | Glucoamylases with N-terminal extensions |
| CN100510067C (zh) * | 1999-07-09 | 2009-07-08 | 诺维信公司 | 葡糖淀粉酶变体 |
| EP2258835A1 (en) * | 2000-04-28 | 2010-12-08 | Novozymes A/S | Lipolytic enzyme variant |
| PL1687419T3 (pl) | 2003-10-28 | 2010-07-30 | Novozymes North America Inc | Enzymy hybrydowe |
-
2000
- 2000-07-07 CN CNB008101329A patent/CN100510067C/zh not_active Expired - Fee Related
- 2000-07-07 AU AU58057/00A patent/AU5805700A/en not_active Abandoned
- 2000-07-07 WO PCT/DK2000/000373 patent/WO2001004273A2/en not_active Ceased
- 2000-07-07 CN CNA2009101412582A patent/CN101550410A/zh active Pending
- 2000-07-07 CA CA002374009A patent/CA2374009A1/en not_active Abandoned
- 2000-07-07 JP JP2001509477A patent/JP2003504046A/ja active Pending
- 2000-07-07 AR ARP000103471A patent/AR029759A1/es active IP Right Grant
- 2000-07-07 EP EP00943688A patent/EP1200566A2/en not_active Ceased
- 2000-07-07 EP EP08159171A patent/EP2009098A1/en not_active Withdrawn
-
2003
- 2003-04-23 US US10/421,586 patent/US7354753B2/en not_active Expired - Fee Related
-
2008
- 2008-02-21 US US12/034,906 patent/US7927857B2/en not_active Expired - Fee Related
- 2008-12-11 AR ARP080105383A patent/AR069653A2/es unknown
-
2011
- 2011-03-01 US US13/037,751 patent/US8722369B2/en not_active Expired - Fee Related
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH05507852A (ja) * | 1990-06-29 | 1993-11-11 | ノボザイムス アクティーゼルスカブ | 遺伝子工学処理をした酵素による澱粉のグルコースへの加水分解 |
| JP2002531121A (ja) * | 1998-12-07 | 2002-09-24 | ノボザイムス アクティーゼルスカブ | N末端伸長を有するグルコアミラーゼ |
| JP2007520047A (ja) * | 2004-01-28 | 2007-07-19 | 東京エレクトロン株式会社 | 大規模誘導結合プラズマ源用の小型な分布型誘導素子 |
Cited By (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007509630A (ja) * | 2003-10-28 | 2007-04-19 | ノボザイムス ノース アメリカ,インコーポレイティド | ハイブリッド酵素 |
| JP2008505632A (ja) * | 2004-07-07 | 2008-02-28 | ダニスコ エイ/エス | 非マルトース生成エキソアミラーゼ改変体 |
| JP2012070751A (ja) * | 2004-07-07 | 2012-04-12 | Danisco As | ポリペプチド |
| JP2014221074A (ja) * | 2004-07-07 | 2014-11-27 | デュポン ニュートリション バイオサイエンシーズ エーピーエス | ポリペプチド |
| CN100443589C (zh) * | 2005-12-30 | 2008-12-17 | 湖南鸿鹰祥生物工程股份有限公司 | 高转化率高纯度糖化酶浓缩液的生产方法 |
| JP2011500020A (ja) * | 2007-10-09 | 2011-01-06 | ダニスコ・ユーエス・インク | 性質が変えられたグルコアミラーゼ変異種 |
| JP2011500019A (ja) * | 2007-10-09 | 2011-01-06 | ダニスコ・ユーエス・インク | グルコアミラーゼ変異体 |
| JP2011502543A (ja) * | 2007-11-20 | 2011-01-27 | ダニスコ・ユーエス・インク | 変更された性質を有するグルコアミラーゼ変異体 |
Also Published As
| Publication number | Publication date |
|---|---|
| CA2374009A1 (en) | 2001-01-18 |
| US20120208243A1 (en) | 2012-08-16 |
| US7354753B2 (en) | 2008-04-08 |
| EP2009098A1 (en) | 2008-12-31 |
| US8722369B2 (en) | 2014-05-13 |
| AU5805700A (en) | 2001-01-30 |
| AR029759A1 (es) | 2003-07-16 |
| AR069653A2 (es) | 2010-02-10 |
| CN100510067C (zh) | 2009-07-08 |
| US20080213843A1 (en) | 2008-09-04 |
| WO2001004273A2 (en) | 2001-01-18 |
| WO2001004273A3 (en) | 2001-09-07 |
| CN101550410A (zh) | 2009-10-07 |
| US7927857B2 (en) | 2011-04-19 |
| US20040002142A1 (en) | 2004-01-01 |
| EP1200566A2 (en) | 2002-05-02 |
| CN1360630A (zh) | 2002-07-24 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2003504046A (ja) | グルコアミラーゼ変異体 | |
| KR100764528B1 (ko) | 글루코아밀라제 변이체 | |
| US8101392B2 (en) | Glucoamylase variants | |
| JP4718005B2 (ja) | 熱安定グルコアミラーゼ | |
| US8222006B2 (en) | Glucoamylase variants | |
| JP2003513666A (ja) | フンガミル様アルファ−アミラーゼ変異体 | |
| US6329186B1 (en) | Glucoamylases with N-terminal extensions | |
| JP2002531121A (ja) | N末端伸長を有するグルコアミラーゼ | |
| EP1914306A2 (en) | Glucoamylase Variants |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20070607 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20070607 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20100323 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20100622 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20100629 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20100910 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20110719 |